Purification of synthetic peptides using reversible chromatographic probes based on the Fmoc molecule

H. L. Ball, P. Mascagni

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

A rapid, versatile, reversible procedure for purifying synthetic peptides has been developed based on the specific incorporation of 4-carboxylate Fmoc derivatives onto the terminal amino acid of peptidyl-resins. The acid stable 4-COR-Fmoc derivatives were synthesised with a variety of chemical groups thus altering the chromatographic properties of the 'target' peptides and permitting their convenient purification, either by reversed-phase HPLC or ion exchange chromatography. The assembly of the peptides involved a capping step to prevent the formation of deletion forms. The 4-COR-Fmoc derivatives were incorporated either as preformed amino acid conjugates or as activated succinimidyl esters. After HF cleavage and purification the 4-COR-Fmoc probes were quantitatively removed with organic bases. The efficiency of the technique was demonstrated by the purification of small to large sized peptides, including a cyclic analogue.

Original languageEnglish (US)
Pages (from-to)370-379
Number of pages10
JournalInternational Journal of Peptide and Protein Research
Volume40
Issue number5
StatePublished - 1992

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Purification
Peptides
Molecules
Derivatives
Amino Acids
Ion Exchange Chromatography
Chromatography
Ion exchange
Esters
Resins
High Pressure Liquid Chromatography
Acids

ASJC Scopus subject areas

  • Biochemistry

Cite this

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abstract = "A rapid, versatile, reversible procedure for purifying synthetic peptides has been developed based on the specific incorporation of 4-carboxylate Fmoc derivatives onto the terminal amino acid of peptidyl-resins. The acid stable 4-COR-Fmoc derivatives were synthesised with a variety of chemical groups thus altering the chromatographic properties of the 'target' peptides and permitting their convenient purification, either by reversed-phase HPLC or ion exchange chromatography. The assembly of the peptides involved a capping step to prevent the formation of deletion forms. The 4-COR-Fmoc derivatives were incorporated either as preformed amino acid conjugates or as activated succinimidyl esters. After HF cleavage and purification the 4-COR-Fmoc probes were quantitatively removed with organic bases. The efficiency of the technique was demonstrated by the purification of small to large sized peptides, including a cyclic analogue.",
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